What is the role of non-native intermediates of β-lactoglobulin in protein folding? | Zendy

George Chikenji | Zendy; Macoto Kikuchi | Zendy

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What is the role of non-native intermediates of β-lactoglobulin in protein folding?

Author(s) -

George Chikenji,

Macoto Kikuchi

Publication year - 2000

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.97.26.14273

Subject(s) - protein folding , energy landscape , folding (dsp implementation) , chemistry , phi value analysis , beta (programming language) , contact order , folding funnel , entropy (arrow of time) , native state , protein structure , biophysics , chemical physics , crystallography , downhill folding , topology (electrical circuits) , biology , biochemistry , physics , computer science , combinatorics , thermodynamics , mathematics , electrical engineering , engineering , programming language

The mechanism of α→β transition in folding of β-lactoglobulin is discussed based on free energy landscape analysis of a long lattice model. It is found that helical propensity of β-lactoglobulin is driven by conformational entropy and is intrinsically coded in its native structure. We propose a view on a role of folding intermediate, which is “on-pathway” but rich in non-native structures. The present results suggest that the native structure topology plays an important role in α→β transition.

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